ENO1 Binds to ApoC3 and Impairs the Proliferation of T Cells via IL-8/STAT3 Pathway in OSCC

Wang, Jing; Man, Qi‐Wen; Zhong, Niannian; Wang, Hanqi; Zhang, Chenxi; Li, Suran; Bu, Lin‐Lin; Liu, Bing

doi:10.3390/ijms232112777

Cited by 3 publications

(1 citation statement)

References 70 publications

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“…Moreover, surface expression of ENO1 has been reported in different cancers, such as in lung, pancreatic and breast cancer. The overexpression of surface ENO1 was related to lymph node metastasis of breast, pancreatic, head and neck cancer and oral squamous cell carcinoma [20][21][22][23][24].…”

Section: Introductionmentioning

confidence: 99%

Identification of the Interaction Domains in the ENO1/Hsp70 Complex, Delve into Novel Potential Therapeutic Target

Gulotta,

Perricone,

Rubino

et al. 2023

Preprint

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Alpha-enolase is a multifunctional protein with oncogenic roles. First described as a glycolytic enzyme the protein performs different functions according to its cellular localization, post-translational modifications, and binding partners. Cell surface-localized alpha-enolase serves as a plasminogen binding receptor and it has been detected in several cell types, including various tumor cells. Plasminogen system plays a crucial role in pathological events such as tumor cell invasion and metastasis. We have previously demonstrated that the interaction of alpha-enolase with the multifunctional chaperone Hsp70 increases its surface localization and the migratory and invasive capacity of breast cancer cells, thus representing a novel potential target to counteract the metastatic potential of tumors. Here we used experimental and computational approaches for the mapping and hot-spot prediction of the interaction domains between alpha-enolase and Hsp70. The molecular definition of this disease-relevant protein-protein interaction will provide the basis for the design of specific inhibitors as potential anti-metastatic agents.

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Section: Introductionmentioning

confidence: 99%

Identification of the Interaction Domains in the ENO1/Hsp70 Complex, Delve into Novel Potential Therapeutic Target

Gulotta,

Perricone,

Rubino

et al. 2023

Preprint

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The role of SEMG1 overexpression in OSCC tumorigenesis and its relation with metabolic molecules

Wang,

Zhong,

et al. 2024

Oral Diseases

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ObjectivesThis study aimed to investigate the expression and biological significance of Semenogelin 1 (SEMG1), a member of the cancer‐testis antigen family, in oral squamous cell carcinoma (OSCC). Further, we explored its potential association with metabolism‐related molecules.MethodsSEMG1 expression levels in OSCC were determined through immunohistochemistry, flow cytometry, and Western blot analyses. To decipher the biological implications of SEMG1 in OSCC, the CAL27 OSCC cell line was either stably overexpressed with SEMG1 or subjected to SEMG1‐shRNA knockdown. The relationship between clinicopathological parameters and SEMG1 expression in OSCC patients was also assessed.ResultsSEMG1 was found to be overexpressed in OSCC, though its expression was not influenced by the pathological grade. The fluorescent dihydroethidium assay indicated that SEMG1 augmented reactive oxygen species production. The mitochondrial membrane potential assay suggested a significant upregulation of mitochondrial membrane potential by SEMG1. Cell cycle assessments highlighted that SEMG1 overexpression led to a notable rise in cells entering the S‐phase. Additionally, a strong correlation between SEMG1 expression and both ENO1 and PKM2 expression in OSCC was observed.ConclusionsThe findings underscore the elevated expression of SEMG1 in OSCC and its contributory role in the tumorigenesis of OSCC patients.

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Role of ENO1 and its targeted therapy in tumors

Li,

Liu,

2024

J Transl Med

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three highly conserved isoforms of enolase in mammals are α-enolase (ENO1), β-enolase (ENO3), and γ-enolase (ENO2). Among them, ENO1 accounts for 90% of the glycolytic pathway's cytosolic enolase activity [3]. Furthermore, ENO1 overexpression is associated with poor prognosis in many types of cancer [4]. ENO2, predominantly localized in the cytoplasm of neurons and neuroendocrine cells, has been identified as a serum marker for tumors of neuronal lineage, such as glioblastoma (GBM) and medulloblastoma [5,6]. Recent studies, however, have revealed that ENO2 is not only highly expressed in neurological tumors but also plays a critical role in the progression of other malignancies, including lung adenocarcinoma (LUAD) and breast cancer. A multiomic analysis demonstrated that 3D tumor spheroid growth implies the overexpression of ENO2 and another glycolytic enzyme, ALDOC, concomitant with the enhanced consumption of glucose and fructose and the enhanced production of lactate, in lung and breast cancer cell lines in different nutrient environmental conditions [7]. ENO3 is predominantly expressed in muscle tissue, with studies indicating that 86% of rhabdomyosarcomas test positive

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ENO1 Binds to ApoC3 and Impairs the Proliferation of T Cells via IL-8/STAT3 Pathway in OSCC

Cited by 3 publications

References 70 publications

Identification of the Interaction Domains in the ENO1/Hsp70 Complex, Delve into Novel Potential Therapeutic Target

Identification of the Interaction Domains in the ENO1/Hsp70 Complex, Delve into Novel Potential Therapeutic Target

The role of SEMG1 overexpression in OSCC tumorigenesis and its relation with metabolic molecules

Role of ENO1 and its targeted therapy in tumors

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